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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Role of Neurotransmitters in Memory01:23

Role of Neurotransmitters in Memory

Neurotransmitters are integral to the brain's communication system, enabling neurons to transmit signals across synapses. This chemical exchange underpins various cognitive functions, including memory processes. The role of neurotransmitters in memory is multifaceted, influencing the encoding, consolidation, and retrieval of memories through their action on different neural circuits.
 Glutamate and Synaptic Plasticity
Glutamate, the brain's main excitatory neurotransmitter, is critical for...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Long-term Potentiation01:35

Long-term Potentiation

Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre- and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.

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Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
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Enhancing memory formation by altering protein phosphorylation balance.

David Rosenegger1, Kashif Parvez, Ken Lukowiak

  • 1Hotchkiss Brain Institute, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, Alta., Canada.

Neurobiology of Learning and Memory
|July 16, 2008
PubMed
Summary
This summary is machine-generated.

Modulating neuronal phosphorylation and dephosphorylation pathways can create long-term memory (LTM) in Lymnaea snails. This involves protein synthesis and gene activity, crucial for memory consolidation.

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

Area of Science:

  • Neuroscience
  • Cellular Biology
  • Behavioral Science

Background:

  • Operant conditioning of aerial respiration in Lymnaea produces intermediate-term memory (ITM) and long-term memory (LTM).
  • ITM requires protein synthesis, while LTM needs both protein synthesis and altered gene activity.
  • A single training session (ITM-training) leaves a molecular trace that can be boosted to LTM with a second training bout.

Purpose of the Study:

  • To investigate the role of neuronal phosphorylation and dephosphorylation in LTM formation.
  • To determine if manipulating these pathways can induce LTM after ITM-training.
  • To confirm the necessity of transcription for LTM formation.

Main Methods:

  • Administering okadaic acid (inhibits protein phosphatase) or bryostatin (increases protein kinase C activity) prior to ITM-training in Lymnaea.
  • Performing ITM-training sessions to assess memory formation.
  • Conducting right pedal dorsal 1 (RPeD1) soma ablation to disrupt transcription and re-evaluating the effects of pharmacological treatments.

Main Results:

  • Inhibiting protein phosphatase or increasing protein kinase C activity prior to ITM-training successfully induced LTM.
  • These treatments were ineffective in producing LTM after RPeD1 soma ablation, indicating transcription is essential.
  • The findings highlight the critical role of the balance between phosphorylation and dephosphorylation.

Conclusions:

  • The balance between neuronal phosphorylation and dephosphorylation is a key factor in LTM formation.
  • Pharmacological manipulation of these pathways can induce LTM, provided transcription is intact.
  • This study provides insights into the molecular mechanisms underlying memory consolidation.